Capillary zone electrophoresis-mass spectrometry of intact proteins

Elena Domínguez-Vega, Rob Haselberg, Govert W. Somsen*

*Corresponding author for this work

Research output: Chapter in Book / Report / Conference proceedingChapterAcademicpeer-review


Capillary electrophoresis (CE) coupled with mass spectrometry (MS) has proven to be a powerful analytical tool for the characterization of intact proteins. It combines the high separation efficiency, short analysis time, and versatility of CE with the mass selectivity and sensitivity offered by MS detection. This chapter focuses on important practical considerations when applying CE-MS for the analysis of intact proteins. Technological aspects with respect to the use of CE-MS interfaces and application of noncovalent capillary coatings preventing protein adsorption are treated. Critical factors for successful protein analysis are discussed and four typical CE-MS systems are described demonstrating the characterization of different types of intact proteins by CE-MS. These methodologies comprise the use of sheath-liquid and sheathless CE-MS interfaces, and various types of noncovalent capillary coatings allowing efficient and reproducible protein separations. The discussion includes the analysis of lysozyme-drug conjugates and the therapeutic proteins human growth hormone, human interferon-β-1a, and human erythropoietin.

Original languageEnglish
Title of host publicationCapillary Electrophoresis of Proteins and Peptides
Subtitle of host publicationMethods and Protocols
EditorsNguyet Thuy Tran, Myriam Taverna
PublisherHumana Press Inc
Number of pages17
ISBN (Electronic)9781493940141
ISBN (Print)9781493940127
Publication statusPublished - 2016

Publication series

NameMethods in Molecular Biology
PublisherHumana Press
ISSN (Print)1064-3745


  • (Non-)covalent coatings
  • Biopharmaceuticals
  • Capillary electrophoresis
  • Electrospray ionization
  • Mass spectrometry
  • Proteins
  • Sheath-liquid interface
  • Sheathless interface


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